DRS2_AGASP
ID DRS2_AGASP Reviewed; 76 AA.
AC A0A5P9K470;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Dermaseptin-SP2 {ECO:0000303|PubMed:31671555};
DE Short=DRS-SP2 {ECO:0000303|PubMed:31671555};
DE Flags: Precursor;
OS Agalychnis spurrelli (Gliding leaf frog) (Agalychnis litodryas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Agalychnis.
OX NCBI_TaxID=317303;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MASS SPECTROMETRY, SYNTHESIS OF
RP 46-73, SUBCELLULAR LOCATION, AND AMIDATION AT GLN-73.
RC TISSUE=Skin secretion;
RX PubMed=31671555; DOI=10.3390/biom9110667;
RA Proano-Bolanos C., Blasco-Zuniga A., Almeida J.R., Wang L.,
RA Llumiquinga M.A., Rivera M., Zhou M., Chen T., Shaw C.;
RT "Unravelling the skin secretion peptides of the gliding leaf frog,
RT Agalychnis spurrelli (Hylidae).";
RL Biomolecules 9:1-20(2019).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SYNTHESIS OF 46-73, IDENTIFICATION BY
RP MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND 3D-STRUCTURE MODELING.
RC TISSUE=Skin secretion;
RX PubMed=31422479; DOI=10.1007/s00894-019-4141-1;
RA Cuesta S., Gallegos F., Arias J., Pilaquinga F., Blasco-Zuniga A.,
RA Proano-Bolanos C., Rivera M., Meneses L.;
RT "Molecular modeling of four dermaseptin-related peptides of the gliding
RT tree frog Agalychnis spurrelli.";
RL J. Mol. Model. 25:260-260(2019).
CC -!- FUNCTION: Antimicrobial peptide with activity against Gram-positive and
CC Gram-negative bacteria and fungi (PubMed:31671555, PubMed:31422479).
CC Has been tested against E.coli (MIC=2.68-8 uM), S.aureus (ATCC 25923,
CC MIC=2.68-8 uM), S.aureus (ATCC oxacillin resistant, MIC=2.68 uM),
CC K.pneumoniae (MIC=10.71 uM) and C.albicans (MIC=10.71-32 uM)
CC (PubMed:31671555, PubMed:31422479). Probably acts by disturbing
CC membrane functions with its alpha-helical amphipathic structure
CC (Probable). May penetrate bacterial membranes, but stay at the
CC mammalian membrane surface (Probable). Shows a very weak hemolytic
CC activity (PubMed:31671555). {ECO:0000269|PubMed:31422479,
CC ECO:0000269|PubMed:31671555, ECO:0000305|PubMed:31422479}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31422479,
CC ECO:0000269|PubMed:31671555}. Target cell membrane
CC {ECO:0000250|UniProtKB:P31107}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:31671555}.
CC -!- MASS SPECTROMETRY: Mass=2988.24; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:31671555};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Dermaseptin subfamily. {ECO:0000305}.
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DR EMBL; MK532480; QFU19630.1; -; mRNA.
DR AlphaFoldDB; A0A5P9K470; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR022731; Dermaseptin.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR InterPro; IPR016322; FSAP.
DR Pfam; PF12121; DD_K; 1.
DR Pfam; PF03032; FSAP_sig_propep; 1.
DR PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Cytolysis; Fungicide; Hemolysis;
KW Immunity; Innate immunity; Membrane; Secreted; Signal;
KW Target cell membrane; Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..45
FT /evidence="ECO:0000305|PubMed:31671555"
FT /id="PRO_0000449983"
FT PEPTIDE 46..73
FT /note="Dermaseptin-SP2"
FT /evidence="ECO:0000269|PubMed:31671555"
FT /id="PRO_0000449984"
FT PROPEP 74..76
FT /evidence="ECO:0000305|PubMed:31671555"
FT /id="PRO_0000449985"
FT REGION 24..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Glutamine amide"
FT /evidence="ECO:0000269|PubMed:31671555"
SQ SEQUENCE 76 AA; 8665 MW; 4DB01755FA3D99BE CRC64;
MAFLKKSLFL VLFLGLVSLS ICEEEKRENE DEEEQEDEEQ SEEKRASWKV FLKNIGKAAG
KAVLNSVTDM VNQGEQ
